Lipid agonism: The PIP2 paradigm of ligand-gated ion channels

• Published in: Biochimica et biophysica acta Vol. 1851; no. 5; pp. 620 - 628
• Main Author: Hansen, Scott B.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2015
• Subjects: agonists; Animals; biophysics; blood proteins; electrophysiology; enzymes; G-protein; Humans; Ion channel; Ion Channel Gating - drug effects; Ligand-Gated Ion Channels - agonists; Ligand-Gated Ion Channels - chemistry; Ligand-Gated Ion Channels - metabolism; Ligands; Lipid gated; Lipid raft; lipids; Membrane Microdomains - drug effects; Membrane Microdomains - metabolism; Membrane Potentials; Models, Molecular; neurotransmitters; pharmacology; Phosphatidylinositol 4,5-Diphosphate - metabolism; PIP2; plasma membrane; potassium channels; Potassium Channels, Inwardly Rectifying - agonists; Potassium Channels, Inwardly Rectifying - chemistry; Potassium Channels, Inwardly Rectifying - metabolism; Protein Conformation; protein structure; Signaling lipid; Structure-Activity Relationship; PS; TREK; PI3 kinase; PTEN; Kv; TRP; Lipid gated; Sn2; Signaling lipid; Ld; AA; Lipid raft; PUFA; VSD; PLA2; ER; HCN; CoA; Kir; P2X; Cav; GPCR; PIP3; GIRK; Mg; PIP2; PLC; BK; Gβγ; PLD; Katp; ASIC; nAChR; NMDA; TM1; G-protein; Ci-VSP; K2P; TMD; DAG; Ion channel; IP3; PA; CTD; MARCKS; PH; PI; ATP; DRM; LAT; C8PIP2; PIP

The past decade, membrane signaling lipids emerged as major regulators of ion channel function. However, the molecular nature of lipid binding to ion channels remained poorly described due to a lack of structural information and assays to quantify and measure lipid binding in a membrane. How does a...